1duk: Difference between revisions

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-[[Image:1duk.gif|left|200px]]
- {{Structure
+==WILD-TYPE RECOMBINANT SPERM WHALE METAQUOMYOGLOBIN==
-|PDB= 1duk |SIZE=350|CAPTION= <scene name='initialview01'>1duk</scene>, resolution 2.13&Aring;
+<StructureSection load='1duk' size='340' side='right'caption='[[1duk]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
+<table><tr><td colspan='2'>[[1duk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DUK FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.13&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1duk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1duk OCA], [https://pdbe.org/1duk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1duk RCSB], [https://www.ebi.ac.uk/pdbsum/1duk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1duk ProSAT]</span></td></tr>
-|RELATEDENTRY=[[1irc|1IRC]], [[1dtm|1DTM]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1duk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1duk OCA], [http://www.ebi.ac.uk/pdbsum/1duk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1duk RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/du/1duk_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1duk ConSurf].
+<div style="clear:both"></div>
-'''WILD-TYPE RECOMBINANT SPERM WHALE METAQUOMYOGLOBIN'''
+==See Also==
+*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
-==Overview==
+__TOC__
-The structural role of a side-chain to side-chain protein hydrogen bond is examined using trans-substitution of the proximal histidine of myoglobin with methylimidazoles (Barrick, Biochemistry 1994;33:6546-6554). Modification of the chemical structure of exogenous ligands allows this hydrogen bond to be disrupted. Comparison of the crystal structures of H93G myoglobin complexed 4-methylimidazole (4meimd; methylation at carbon 4) and 1-methylimidazole (1meimd; methylation at the adjacent nitrogen, preventing hydrogen bonding between the imidazole ligand and the protein) shows that the polypeptide, heme, and methylimidazole orientations are the same within error. For 4meimd there appear to be major and minor conformations corresponding to different tautomeric states of the ligand. Conformational heterogeneity is also seen in the hyperfine-shifted region of the NMR spectrum of 4meimd complexed with high-spin H93G deoxyMb. The major conformation of the 4meimd ligand and the 1meimd ligand, as seen in the respective crystal structures, are quite similar except that the proximal ligand NH-to-Ser92-OH hydrogen bond is eliminated in the 1meimd complex, and instead the proximal ligand CH is adjacent to the Ser92-OH. Thus, this system provides a means to eliminate the Mb proximal hydrogen bond in a chemically and structurally conservative way.
+</StructureSection>
+[[Category: Large Structures]]
-==About this Structure==
-DUK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUK OCA].
-==Reference==
-Trans-substitution of the proximal hydrogen bond in myoglobin: I. Structural consequences of hydrogen bond deletion., Barrick D, Dahlquist FW, Proteins. 2000 Jun 1;39(4):278-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10813811 10813811]
 [[Category: Physeter catodon]]
-[[Category: Single protein]]
+[[Category: Barrick D]]
-[[Category: Barrick, D.]]
+[[Category: Dahlquist FW]]
-[[Category: Dahlquist, F W.]]
-[[Category: heme protein]]
-[[Category: myoglobin]]
-[[Category: oxygen-storage protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:57 2008''